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P08514

- ITA2B_HUMAN

UniProt

P08514 - ITA2B_HUMAN

Protein

Integrin alpha-IIb

Gene

ITGA2B

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 190 (01 Oct 2014)
      Sequence version 3 (14 Apr 2009)
      Previous versions | rss
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    Functioni

    Integrin alpha-IIb/beta-3 is a receptor for fibronectin, fibrinogen, plasminogen, prothrombin, thrombospondin and vitronectin. It recognizes the sequence R-G-D in a wide array of ligands. It recognizes the sequence H-H-L-G-G-G-A-K-Q-A-G-D-V in fibrinogen gamma chain. Following activation integrin alpha-IIb/beta-3 brings about platelet/platelet interaction through binding of soluble fibrinogen. This step leads to rapid platelet aggregation which physically plugs ruptured endothelial cell surface.

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Calcium bindingi274 – 2829Sequence Analysis
    Calcium bindingi328 – 3369Sequence Analysis
    Calcium bindingi396 – 4049Sequence Analysis
    Calcium bindingi457 – 4659Sequence Analysis

    GO - Molecular functioni

    1. extracellular matrix binding Source: Ensembl
    2. identical protein binding Source: IntAct
    3. metal ion binding Source: UniProtKB-KW
    4. protein binding Source: IntAct

    GO - Biological processi

    1. axon guidance Source: Reactome
    2. blood coagulation Source: Reactome
    3. cell adhesion Source: ProtInc
    4. cell-matrix adhesion Source: Ensembl
    5. extracellular matrix organization Source: Reactome
    6. integrin-mediated signaling pathway Source: UniProtKB-KW
    7. platelet activation Source: Reactome
    8. platelet aggregation Source: Ensembl
    9. platelet degranulation Source: Reactome
    10. positive regulation of leukocyte migration Source: Ensembl

    Keywords - Molecular functioni

    Integrin, Receptor

    Keywords - Biological processi

    Cell adhesion

    Keywords - Ligandi

    Calcium, Metal-binding

    Enzyme and pathway databases

    ReactomeiREACT_13552. Integrin cell surface interactions.
    REACT_15381. p130Cas linkage to MAPK signaling for integrins.
    REACT_15523. Integrin alphaIIb beta3 signaling.
    REACT_163906. ECM proteoglycans.
    REACT_22272. Signal transduction by L1.
    SignaLinkiP08514.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Integrin alpha-IIb
    Alternative name(s):
    GPalpha IIb
    Short name:
    GPIIb
    Platelet membrane glycoprotein IIb
    CD_antigen: CD41
    Cleaved into the following 3 chains:
    Gene namesi
    Name:ITGA2B
    Synonyms:GP2B, ITGAB
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:6138. ITGA2B.

    Subcellular locationi

    GO - Cellular componenti

    1. blood microparticle Source: UniProt
    2. external side of plasma membrane Source: Ensembl
    3. extracellular vesicular exosome Source: UniProtKB
    4. focal adhesion Source: Ensembl
    5. integral component of plasma membrane Source: ProtInc
    6. integrin complex Source: InterPro
    7. plasma membrane Source: Reactome
    8. platelet alpha granule membrane Source: Reactome

    Keywords - Cellular componenti

    Membrane

    Pathology & Biotechi

    Involvement in diseasei

    Glanzmann thrombasthenia (GT) [MIM:273800]: A common inherited disease of platelet aggregation. It is characterized by mucocutaneous bleeding of mild-to-moderate severity. GT has been classified clinically into types I and II. In type I, platelets show absence of the glycoprotein IIb-IIIa complexes at their surface and lack fibrinogen and clot retraction capability. In type II, the platelets express the GPIIb-IIIa complex at reduced levels, have detectable amounts of fibrinogen, and have low or moderate clot retraction capability.20 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti86 – 861L → P in GT; cells co-transfected with mutated alpha-IIb and wild-type beta-3 scarcely expressed the alpha-IIb/beta-3 complex. 1 Publication
    VAR_030445
    Natural varianti139 – 1391A → V in GT. 1 Publication
    VAR_030446
    Natural varianti161 – 1611C → W in GT. 1 Publication
    VAR_030447
    Natural varianti174 – 1741Y → H in GT; abolishes the binding function of alpha-IIb/beta-3 for soluble ligands without disturbing alpha-IIb/beta-3 expression; functional defect is likely caused by its allosteric effect rather than by a defect in the ligand-binding site itself. 1 Publication
    VAR_030448
    Natural varianti176 – 1761P → A in GT; impairs surface expression of alpha-IIb/beta-3 and abrogates ligand binding to the activated integrin. 2 Publications
    VAR_009885
    Natural varianti176 – 1761P → L in GT; impairs surface expression of alpha-IIb/beta-3. 1 Publication
    VAR_009886
    Natural varianti202 – 2021F → C in GT; associated with abrogation of alpha-IIb/beta-3 complex formation. 1 Publication
    VAR_030449
    Natural varianti207 – 2071T → I in GT. 1 Publication
    VAR_030450
    Natural varianti214 – 2141L → P in GT; disrupts the structural conformation and the ligand binding properties of the heterodimeric complex; in addition the mutation appears to confer susceptibility to proteolysis. 1 Publication
    VAR_030451
    Natural varianti222 – 2221F → L in GT. 1 Publication
    VAR_030452
    Natural varianti267 – 2671G → E in GT. 1 Publication
    VAR_030453
    Natural varianti273 – 2731G → D in GT; alters the heterodimer conformation thus impairing their intracellular transport. 1 Publication
    VAR_003979
    Natural varianti320 – 3201F → S in GT; type I; impairs surface expression of alpha-IIb/beta-3. 1 Publication
    VAR_009887
    Natural varianti329 – 3291V → F in GT; expression of mutant subunit alpha-IIb/bet-3 is 28% of control; mutant pro-alpha-IIb subunit is retained in the endoplasmic reticulum. 1 Publication
    VAR_030454
    Natural varianti355 – 3551E → K in GT; type I; impairs surface expression of alpha-IIb/beta-3. 2 Publications
    VAR_009888
    Natural varianti358 – 3581R → H in GT; type II. 1 Publication
    VAR_003980
    Natural varianti380 – 3801G → D in GT. 1 Publication
    VAR_030455
    Natural varianti405 – 4051I → T in GT; expression of mutant subunit alpha-IIb/bet-3 is 11% of control; mutant pro-alpha-IIb subunit is retained in the endoplasmic reticulum. 3 Publications
    VAR_030456
    Natural varianti412 – 4121G → R in GT. 1 Publication
    VAR_030457
    Natural varianti449 – 4491G → D in GT; type I. 1 Publication
    VAR_003981
    Natural varianti456 – 4572Missing in GT; alteres the conformation of heterodimers such that they were neither recognized by the heterodimer-specific antibody A2A9 nor able to undergo further intracellular processing or transport to the cell surface.
    VAR_030458
    Natural varianti581 – 5811A → D in GT. 1 Publication
    VAR_030459
    Natural varianti596 – 5961I → T in GT; type I. 3 Publications
    VAR_030460
    Natural varianti705 – 7051C → R in GT; type II; the rate of subunit maturation and the surface exposure of ghlycoprotein IIb/beta-3 are strongly reduced. 3 Publications
    VAR_030461
    Natural varianti752 – 7521L → V in GT. 1 Publication
    VAR_030462
    Natural varianti755 – 7551R → P in GT. 1 Publication
    VAR_030463
    Natural varianti778 – 7781Q → P in GT; type II. 3 Publications
    VAR_003982
    Natural varianti847 – 8471L → P in GT. 1 Publication
    VAR_030464
    Natural varianti934 – 9341V → F in GT; the mutation prevented normal ITGA2B/ITGB3 complex expression on the cell surface consistent with a severe type 1 phenotype. 1 Publication
    VAR_069917
    Natural varianti943 – 9431P → L in GT; marked reduction in the rate of surface expression. 1 Publication
    VAR_030465
    Natural varianti957 – 9571S → L in GT; the mutation prevented normal ITGA2B/ITGB3 complex expression on the cell surface consistent with a severe type 1 phenotype; the mutation may interfere with correct folding of the protein. 1 Publication
    VAR_069918
    Natural varianti982 – 9821V → M in GT; much reduced surface expression of alpha-IIb/beta-3 and a block in the maturation of pro-alpha-IIb. 2 Publications
    VAR_030466
    Natural varianti1026 – 10261R → Q in GT and BDPLT16; results in low surface expression of the mutant protein. 2 Publications
    VAR_030468
    Bleeding disorder, platelet-type 16 (BDPLT16) [MIM:187800]: An autosomal dominant form of congenital macrothrombocytopenia associated with platelet anisocytosis. It is a disorder of platelet production. Affected individuals may have no or only mildly increased bleeding tendency. In vitro studies show mild platelet functional abnormalities.2 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti1026 – 10261R → Q in GT and BDPLT16; results in low surface expression of the mutant protein. 2 Publications
    VAR_030468
    Natural varianti1026 – 10261R → W in BDPLT16; results in abnormal membrane ruffling and cytoplasmic protrusions as well as defective proplatelet formation. 1 Publication
    VAR_069919

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi1029 – 10302PP → AA: Imparts constitutive activity (ligand-binding) to alpha-IIb/beta-3. 1 Publication

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi187800. phenotype.
    273800. phenotype.
    Orphaneti140957. Autosomal dominant macrothrombocytopenia.
    853. Fetal and neonatal alloimmune thrombocytopenia.
    849. Glanzmann thrombasthenia.
    PharmGKBiPA29938.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 31313 PublicationsAdd
    BLAST
    Chaini32 – 10391008Integrin alpha-IIbPRO_0000016275Add
    BLAST
    Chaini32 – 887856Integrin alpha-IIb heavy chainPRO_0000016276Add
    BLAST
    Chaini891 – 1039149Integrin alpha-IIb light chain, form 1PRO_0000292348Add
    BLAST
    Chaini903 – 1039137Integrin alpha-IIb light chain, form 2PRO_0000016277Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi46 – 461N-linked (GlcNAc...)1 Publication
    Disulfide bondi87 ↔ 961 Publication
    Disulfide bondi138 ↔ 1611 Publication
    Disulfide bondi177 ↔ 1981 Publication
    Glycosylationi280 – 2801N-linked (GlcNAc...)1 Publication
    Disulfide bondi504 ↔ 5151 Publication
    Disulfide bondi521 ↔ 5761 Publication
    Glycosylationi601 – 6011N-linked (GlcNAc...)2 Publications
    Disulfide bondi633 ↔ 6391 Publication
    Disulfide bondi705 ↔ 7181 Publication
    Glycosylationi711 – 7111N-linked (GlcNAc...)1 Publication
    Disulfide bondi857 ↔ 911Interchain (between heavy and light chains)1 Publication
    Glycosylationi874 – 8741O-linked (GalNAc...); in alloantigen HPA-3B
    Glycosylationi878 – 8781O-linked (GalNAc...)1 Publication
    Modified residuei891 – 8911Pyrrolidone carboxylic acid; in light chain form 11 Publication
    Disulfide bondi916 ↔ 9211 Publication
    Glycosylationi962 – 9621N-linked (GlcNAc...)

    Keywords - PTMi

    Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, Pyrrolidone carboxylic acid

    Proteomic databases

    PaxDbiP08514.
    PRIDEiP08514.

    2D gel databases

    OGPiP08514.

    PTM databases

    PhosphoSiteiP08514.

    Miscellaneous databases

    PMAP-CutDBQ17R67.

    Expressioni

    Tissue specificityi

    Isoform 1 and isoform 2 were identified in platelets and megakaryocytes, but not in reticulocytes or in Jurkat and U-937 white blood cell line. Isoform 3 is expressed by leukemia, prostate adenocarcinoma and melanoma cells but not by platelets or normal prostate or breast epithelial cells.

    Gene expression databases

    ArrayExpressiP08514.
    BgeeiP08514.
    CleanExiHS_ITGA2B.
    GenevestigatoriP08514.

    Organism-specific databases

    HPAiCAB018611.
    HPA031168.
    HPA031169.
    HPA031170.
    HPA031171.

    Interactioni

    Subunit structurei

    Heterodimer of an alpha and a beta subunit. The alpha subunit is composed of a heavy and a light chain linked by a disulfide bond. Alpha-IIb associates with beta-3. Directly interacts with RNF181. Interacts (via C-terminus cytoplasmic tail region) with CIB1; the interaction is direct and calcium-dependent. Interacts (via C-terminus cytoplasmic tail region) with CIB2, CIB3 and CIB4; the interactions are stabilized/increased in a calcium and magnesium-dependent manner.6 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself7EBI-702693,EBI-702693
    ITGB3P0510611EBI-702693,EBI-702847

    Protein-protein interaction databases

    BioGridi109881. 10 interactions.
    DIPiDIP-68N.
    IntActiP08514. 1 interaction.
    STRINGi9606.ENSP00000262407.

    Structurei

    Secondary structure

    1
    1039
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi36 – 383
    Beta strandi40 – 434
    Beta strandi52 – 587
    Beta strandi60 – 623
    Beta strandi64 – 707
    Beta strandi78 – 803
    Beta strandi82 – 887
    Beta strandi93 – 953
    Beta strandi107 – 1104
    Beta strandi113 – 1186
    Beta strandi126 – 1316
    Beta strandi134 – 1396
    Beta strandi143 – 1486
    Beta strandi151 – 1533
    Beta strandi160 – 1645
    Turni166 – 1683
    Beta strandi171 – 1744
    Helixi183 – 1886
    Turni189 – 1935
    Beta strandi202 – 2065
    Beta strandi211 – 2166
    Helixi219 – 2224
    Beta strandi225 – 2306
    Helixi231 – 2377
    Helixi259 – 2613
    Beta strandi268 – 2736
    Beta strandi279 – 2813
    Beta strandi283 – 2886
    Helixi291 – 2944
    Beta strandi297 – 3015
    Beta strandi307 – 3126
    Beta strandi324 – 3274
    Beta strandi330 – 3334
    Beta strandi336 – 3416
    Beta strandi345 – 3484
    Turni349 – 3513
    Beta strandi352 – 3554
    Beta strandi358 – 3625
    Beta strandi366 – 3683
    Beta strandi375 – 3795
    Beta strandi391 – 3955
    Beta strandi400 – 4023
    Beta strandi404 – 4096
    Beta strandi413 – 4175
    Beta strandi419 – 4235
    Beta strandi427 – 4304
    Beta strandi435 – 4395
    Beta strandi450 – 4567
    Beta strandi458 – 4636
    Beta strandi465 – 4706
    Helixi471 – 4733
    Beta strandi475 – 4795
    Beta strandi484 – 49310
    Beta strandi507 – 5093
    Beta strandi512 – 52514
    Beta strandi534 – 5418
    Turni542 – 5443
    Helixi547 – 5493
    Beta strandi551 – 5544
    Turni555 – 5573
    Beta strandi559 – 5679
    Beta strandi575 – 5839
    Helixi586 – 5883
    Beta strandi596 – 6038
    Beta strandi616 – 6194
    Beta strandi622 – 6276
    Turni634 – 6374
    Beta strandi643 – 6519
    Beta strandi653 – 6553
    Beta strandi662 – 6709
    Beta strandi678 – 6836
    Beta strandi688 – 6958
    Beta strandi705 – 7084
    Beta strandi710 – 7134
    Beta strandi715 – 7217
    Beta strandi728 – 73811
    Beta strandi746 – 75510
    Beta strandi759 – 7613
    Beta strandi767 – 7748
    Beta strandi779 – 79214
    Beta strandi810 – 81910
    Beta strandi821 – 8233
    Beta strandi825 – 83612
    Beta strandi842 – 85413
    Beta strandi856 – 8616
    Beta strandi906 – 9094
    Turni911 – 9133
    Beta strandi916 – 92611
    Beta strandi931 – 94010
    Helixi942 – 9454
    Beta strandi952 – 96514
    Beta strandi967 – 9693
    Beta strandi977 – 98812
    Turni991 – 9944
    Helixi997 – 102024
    Beta strandi1022 – 10243
    Turni1025 – 10273
    Helixi1028 – 10314
    Turni1035 – 10384

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1DPKNMR-A1020-1039[»]
    1DPQNMR-A1020-1039[»]
    1JX5model-A32-483[»]
    1KUPNMR-A1018-1028[»]
    1KUZNMR-A1018-1028[»]
    1M8ONMR-A1020-1039[»]
    1RN0model-A32-482[»]
    1S4WNMR-A1020-1039[»]
    1TYEX-ray2.90A/C/E32-483[»]
    1UV9model-A32-973[»]
    2K1ANMR-A989-1029[»]
    2K9JNMR-A989-1029[»]
    2KNCNMR-A991-1039[»]
    2VC2X-ray3.10A32-483[»]
    2VDKX-ray2.80A32-483[»]
    2VDLX-ray2.75A32-483[»]
    2VDMX-ray2.90A32-483[»]
    2VDNX-ray2.90A32-483[»]
    2VDOX-ray2.51A32-483[»]
    2VDPX-ray2.80A32-483[»]
    2VDQX-ray2.59A32-483[»]
    2VDRX-ray2.40A32-483[»]
    3FCSX-ray2.55A/C32-989[»]
    3FCUX-ray2.90A/C/E32-488[»]
    3NIDX-ray2.30A/C32-488[»]
    3NIFX-ray2.40A/C32-488[»]
    3NIGX-ray2.25A/C32-488[»]
    3T3MX-ray2.60A/C32-488[»]
    3T3PX-ray2.20A/C32-488[»]
    3ZDXX-ray2.45A/C32-488[»]
    3ZDYX-ray2.45A/C32-488[»]
    3ZDZX-ray2.75A/C32-488[»]
    3ZE0X-ray2.95A/C32-488[»]
    3ZE1X-ray3.00A/C32-488[»]
    3ZE2X-ray2.35A/C32-488[»]
    4CAKelectron microscopy20.50A32-989[»]
    ProteinModelPortaliP08514.
    SMRiP08514. Positions 32-989, 991-1039.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP08514.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini32 – 993962ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini1020 – 103920CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei994 – 101926HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati35 – 9662FG-GAP 1Add
    BLAST
    Repeati110 – 17364FG-GAP 2Add
    BLAST
    Repeati186 – 23853FG-GAP 3Add
    BLAST
    Repeati251 – 31060FG-GAP 4Add
    BLAST
    Repeati311 – 37161FG-GAP 5Add
    BLAST
    Repeati373 – 43260FG-GAP 6Add
    BLAST
    Repeati434 – 49663FG-GAP 7Add
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi1022 – 10265GFFKR motif

    Sequence similaritiesi

    Belongs to the integrin alpha chain family.Curated
    Contains 7 FG-GAP repeats.Curated

    Keywords - Domaini

    Repeat, Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG26407.
    HOGENOMiHOG000231603.
    HOVERGENiHBG006186.
    InParanoidiP08514.
    KOiK06476.
    OMAiCFNIQMC.
    OrthoDBiEOG7TMZQZ.
    PhylomeDBiP08514.
    TreeFamiTF105391.

    Family and domain databases

    InterProiIPR013517. FG-GAP.
    IPR013519. Int_alpha_beta-p.
    IPR000413. Integrin_alpha.
    IPR013649. Integrin_alpha-2.
    IPR018184. Integrin_alpha_C_CS.
    [Graphical view]
    PfamiPF01839. FG-GAP. 1 hit.
    PF00357. Integrin_alpha. 1 hit.
    PF08441. Integrin_alpha2. 1 hit.
    [Graphical view]
    PRINTSiPR01185. INTEGRINA.
    SMARTiSM00191. Int_alpha. 5 hits.
    [Graphical view]
    PROSITEiPS51470. FG_GAP. 7 hits.
    PS00242. INTEGRIN_ALPHA. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P08514-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MARALCPLQA LWLLEWVLLL LGPCAAPPAW ALNLDPVQLT FYAGPNGSQF     50
    GFSLDFHKDS HGRVAIVVGA PRTLGPSQEE TGGVFLCPWR AEGGQCPSLL 100
    FDLRDETRNV GSQTLQTFKA RQGLGASVVS WSDVIVACAP WQHWNVLEKT 150
    EEAEKTPVGS CFLAQPESGR RAEYSPCRGN TLSRIYVEND FSWDKRYCEA 200
    GFSSVVTQAG ELVLGAPGGY YFLGLLAQAP VADIFSSYRP GILLWHVSSQ 250
    SLSFDSSNPE YFDGYWGYSV AVGEFDGDLN TTEYVVGAPT WSWTLGAVEI 300
    LDSYYQRLHR LRGEQMASYF GHSVAVTDVN GDGRHDLLVG APLYMESRAD 350
    RKLAEVGRVY LFLQPRGPHA LGAPSLLLTG TQLYGRFGSA IAPLGDLDRD 400
    GYNDIAVAAP YGGPSGRGQV LVFLGQSEGL RSRPSQVLDS PFPTGSAFGF 450
    SLRGAVDIDD NGYPDLIVGA YGANQVAVYR AQPVVKASVQ LLVQDSLNPA 500
    VKSCVLPQTK TPVSCFNIQM CVGATGHNIP QKLSLNAELQ LDRQKPRQGR 550
    RVLLLGSQQA GTTLNLDLGG KHSPICHTTM AFLRDEADFR DKLSPIVLSL 600
    NVSLPPTEAG MAPAVVLHGD THVQEQTRIV LDCGEDDVCV PQLQLTASVT 650
    GSPLLVGADN VLELQMDAAN EGEGAYEAEL AVHLPQGAHY MRALSNVEGF 700
    ERLICNQKKE NETRVVLCEL GNPMKKNAQI GIAMLVSVGN LEEAGESVSF 750
    QLQIRSKNSQ NPNSKIVLLD VPVRAEAQVE LRGNSFPASL VVAAEEGERE 800
    QNSLDSWGPK VEHTYELHNN GPGTVNGLHL SIHLPGQSQP SDLLYILDIQ 850
    PQGGLQCFPQ PPVNPLKVDW GLPIPSPSPI HPAHHKRDRR QIFLPEPEQP 900
    SRLQDPVLVS CDSAPCTVVQ CDLQEMARGQ RAMVTVLAFL WLPSLYQRPL 950
    DQFVLQSHAW FNVSSLPYAV PPLSLPRGEA QVWTQLLRAL EERAIPIWWV 1000
    LVGVLGGLLL LTILVLAMWK VGFFKRNRPP LEEDDEEGE 1039
    Length:1,039
    Mass (Da):113,377
    Last modified:April 14, 2009 - v3
    Checksum:i063EE298E026F116
    GO
    Isoform 2 (identifier: P08514-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         948-981: Missing.

    Show »
    Length:1,005
    Mass (Da):109,574
    Checksum:i81C09F0D904CB534
    GO
    Isoform 3 (identifier: P08514-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         910-1039: SCDSAPCTVV...PLEEDDEEGE → VSRLSGLWPG...ATLGPWEHFK

    Show »
    Length:953
    Mass (Da):103,218
    Checksum:i0100D4C5919320BE
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti23 – 231P → A in AAA35926. (PubMed:2345548)Curated
    Sequence conflicti120 – 1201A → S in BAG37735. (PubMed:14702039)Curated
    Sequence conflicti287 – 2882GA → VP in AAA53150. (PubMed:2322558)Curated
    Sequence conflicti346 – 3461E → D in AAA35926. (PubMed:2345548)Curated
    Sequence conflicti565 – 5651N → D in AAA35926. (PubMed:2345548)Curated
    Sequence conflicti566 – 5661L → V in CAA29987. (PubMed:3422188)Curated
    Sequence conflicti633 – 6331C → S in AAA60114. (PubMed:2439501)Curated
    Sequence conflicti729 – 7291Q → E in CAA29987. (PubMed:3422188)Curated
    Sequence conflicti971 – 9711P → A in AAA53150. (PubMed:2322558)Curated
    Sequence conflicti1029 – 10291P → H in AAA35926. (PubMed:2345548)Curated
    Sequence conflicti1029 – 10291P → H in AAA52588. (PubMed:2845986)Curated
    Sequence conflicti1030 – 10301P → T in AAA52588. (PubMed:2845986)Curated

    Polymorphismi

    Position 874 is associated with platelet-specific alloantigen HPA-3/BAK/LEK. HPA-3A/BAK(A)/LEK(A) has Ile-874 and HPA-3B/BAK(B)/LEK(B) has Ser-874. HPA-3B is involved in neonatal alloimmune thrombocytopenia (NAIT or NATP).

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti40 – 401T → I.1 Publication
    Corresponds to variant rs5915 [ dbSNP | Ensembl ].
    VAR_014176
    Natural varianti86 – 861L → P in GT; cells co-transfected with mutated alpha-IIb and wild-type beta-3 scarcely expressed the alpha-IIb/beta-3 complex. 1 Publication
    VAR_030445
    Natural varianti139 – 1391A → V in GT. 1 Publication
    VAR_030446
    Natural varianti161 – 1611C → W in GT. 1 Publication
    VAR_030447
    Natural varianti174 – 1741Y → H in GT; abolishes the binding function of alpha-IIb/beta-3 for soluble ligands without disturbing alpha-IIb/beta-3 expression; functional defect is likely caused by its allosteric effect rather than by a defect in the ligand-binding site itself. 1 Publication
    VAR_030448
    Natural varianti176 – 1761P → A in GT; impairs surface expression of alpha-IIb/beta-3 and abrogates ligand binding to the activated integrin. 2 Publications
    VAR_009885
    Natural varianti176 – 1761P → L in GT; impairs surface expression of alpha-IIb/beta-3. 1 Publication
    VAR_009886
    Natural varianti202 – 2021F → C in GT; associated with abrogation of alpha-IIb/beta-3 complex formation. 1 Publication
    VAR_030449
    Natural varianti207 – 2071T → I in GT. 1 Publication
    VAR_030450
    Natural varianti214 – 2141L → P in GT; disrupts the structural conformation and the ligand binding properties of the heterodimeric complex; in addition the mutation appears to confer susceptibility to proteolysis. 1 Publication
    VAR_030451
    Natural varianti222 – 2221F → L in GT. 1 Publication
    VAR_030452
    Natural varianti267 – 2671G → E in GT. 1 Publication
    VAR_030453
    Natural varianti273 – 2731G → D in GT; alters the heterodimer conformation thus impairing their intracellular transport. 1 Publication
    VAR_003979
    Natural varianti313 – 3131G → A.2 Publications
    Corresponds to variant rs1126554 [ dbSNP | Ensembl ].
    VAR_054820
    Natural varianti320 – 3201F → S in GT; type I; impairs surface expression of alpha-IIb/beta-3. 1 Publication
    VAR_009887
    Natural varianti329 – 3291V → F in GT; expression of mutant subunit alpha-IIb/bet-3 is 28% of control; mutant pro-alpha-IIb subunit is retained in the endoplasmic reticulum. 1 Publication
    VAR_030454
    Natural varianti355 – 3551E → K in GT; type I; impairs surface expression of alpha-IIb/beta-3. 2 Publications
    VAR_009888
    Natural varianti358 – 3581R → H in GT; type II. 1 Publication
    VAR_003980
    Natural varianti380 – 3801G → D in GT. 1 Publication
    VAR_030455
    Natural varianti405 – 4051I → T in GT; expression of mutant subunit alpha-IIb/bet-3 is 11% of control; mutant pro-alpha-IIb subunit is retained in the endoplasmic reticulum. 3 Publications
    VAR_030456
    Natural varianti412 – 4121G → R in GT. 1 Publication
    VAR_030457
    Natural varianti449 – 4491G → D in GT; type I. 1 Publication
    VAR_003981
    Natural varianti456 – 4572Missing in GT; alteres the conformation of heterodimers such that they were neither recognized by the heterodimer-specific antibody A2A9 nor able to undergo further intracellular processing or transport to the cell surface.
    VAR_030458
    Natural varianti581 – 5811A → D in GT. 1 Publication
    VAR_030459
    Natural varianti596 – 5961I → T in GT; type I. 3 Publications
    VAR_030460
    Natural varianti649 – 6491V → L.
    Corresponds to variant rs7207402 [ dbSNP | Ensembl ].
    VAR_054821
    Natural varianti705 – 7051C → R in GT; type II; the rate of subunit maturation and the surface exposure of ghlycoprotein IIb/beta-3 are strongly reduced. 3 Publications
    VAR_030461
    Natural varianti752 – 7521L → V in GT. 1 Publication
    VAR_030462
    Natural varianti755 – 7551R → P in GT. 1 Publication
    VAR_030463
    Natural varianti778 – 7781Q → P in GT; type II. 3 Publications
    VAR_003982
    Natural varianti847 – 8471L → P in GT. 1 Publication
    VAR_030464
    Natural varianti874 – 8741I → S Alloantigen HPA-3B. 1 Publication
    Corresponds to variant rs5911 [ dbSNP | Ensembl ].
    VAR_003983
    Natural varianti934 – 9341V → F in GT; the mutation prevented normal ITGA2B/ITGB3 complex expression on the cell surface consistent with a severe type 1 phenotype. 1 Publication
    VAR_069917
    Natural varianti943 – 9431P → L in GT; marked reduction in the rate of surface expression. 1 Publication
    VAR_030465
    Natural varianti957 – 9571S → L in GT; the mutation prevented normal ITGA2B/ITGB3 complex expression on the cell surface consistent with a severe type 1 phenotype; the mutation may interfere with correct folding of the protein. 1 Publication
    VAR_069918
    Natural varianti968 – 9681Y → N.1 Publication
    Corresponds to variant rs5914 [ dbSNP | Ensembl ].
    VAR_014177
    Natural varianti982 – 9821V → M in GT; much reduced surface expression of alpha-IIb/beta-3 and a block in the maturation of pro-alpha-IIb. 2 Publications
    VAR_030466
    Natural varianti989 – 9891A → T.2 Publications
    Corresponds to variant rs78165611 [ dbSNP | Ensembl ].
    VAR_030467
    Natural varianti1026 – 10261R → Q in GT and BDPLT16; results in low surface expression of the mutant protein. 2 Publications
    VAR_030468
    Natural varianti1026 – 10261R → W in BDPLT16; results in abnormal membrane ruffling and cytoplasmic protrusions as well as defective proplatelet formation. 1 Publication
    VAR_069919

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei910 – 1039130SCDSA…DEEGE → VSRLSGLWPGLPGTHGAEGM GGGRGVRVCCGPLWATLGPW EHFK in isoform 3. CuratedVSP_002736Add
    BLAST
    Alternative sequencei948 – 98134Missing in isoform 2. CuratedVSP_002737Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J02764 mRNA. Translation: AAA60114.1.
    M34480 mRNA. Translation: AAA35926.1.
    M34344, M33319, M33320 Genomic DNA. Translation: AAA53150.1.
    M54799 Genomic DNA. Translation: AAA52599.1.
    X06831 mRNA. Translation: CAA29987.1.
    M18085 mRNA. Translation: AAA52597.1.
    M22568 Genomic DNA. Translation: AAA52587.1.
    M22569 Genomic DNA. Translation: AAA52588.1.
    AF098114 mRNA. Translation: AAC98507.1.
    AK315335 mRNA. Translation: BAG37735.1.
    AC003043 Genomic DNA. No translation available.
    BC117443 mRNA. Translation: AAI17444.1.
    BC126442 mRNA. Translation: AAI26443.1.
    CCDSiCCDS32665.1. [P08514-1]
    PIRiA34269.
    RefSeqiNP_000410.2. NM_000419.3. [P08514-1]
    UniGeneiHs.411312.

    Genome annotation databases

    EnsembliENST00000262407; ENSP00000262407; ENSG00000005961. [P08514-1]
    GeneIDi3674.
    KEGGihsa:3674.
    UCSCiuc002igt.1. human. [P08514-1]

    Polymorphism databases

    DMDMi226694183.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J02764 mRNA. Translation: AAA60114.1 .
    M34480 mRNA. Translation: AAA35926.1 .
    M34344 , M33319 , M33320 Genomic DNA. Translation: AAA53150.1 .
    M54799 Genomic DNA. Translation: AAA52599.1 .
    X06831 mRNA. Translation: CAA29987.1 .
    M18085 mRNA. Translation: AAA52597.1 .
    M22568 Genomic DNA. Translation: AAA52587.1 .
    M22569 Genomic DNA. Translation: AAA52588.1 .
    AF098114 mRNA. Translation: AAC98507.1 .
    AK315335 mRNA. Translation: BAG37735.1 .
    AC003043 Genomic DNA. No translation available.
    BC117443 mRNA. Translation: AAI17444.1 .
    BC126442 mRNA. Translation: AAI26443.1 .
    CCDSi CCDS32665.1. [P08514-1 ]
    PIRi A34269.
    RefSeqi NP_000410.2. NM_000419.3. [P08514-1 ]
    UniGenei Hs.411312.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1DPK NMR - A 1020-1039 [» ]
    1DPQ NMR - A 1020-1039 [» ]
    1JX5 model - A 32-483 [» ]
    1KUP NMR - A 1018-1028 [» ]
    1KUZ NMR - A 1018-1028 [» ]
    1M8O NMR - A 1020-1039 [» ]
    1RN0 model - A 32-482 [» ]
    1S4W NMR - A 1020-1039 [» ]
    1TYE X-ray 2.90 A/C/E 32-483 [» ]
    1UV9 model - A 32-973 [» ]
    2K1A NMR - A 989-1029 [» ]
    2K9J NMR - A 989-1029 [» ]
    2KNC NMR - A 991-1039 [» ]
    2VC2 X-ray 3.10 A 32-483 [» ]
    2VDK X-ray 2.80 A 32-483 [» ]
    2VDL X-ray 2.75 A 32-483 [» ]
    2VDM X-ray 2.90 A 32-483 [» ]
    2VDN X-ray 2.90 A 32-483 [» ]
    2VDO X-ray 2.51 A 32-483 [» ]
    2VDP X-ray 2.80 A 32-483 [» ]
    2VDQ X-ray 2.59 A 32-483 [» ]
    2VDR X-ray 2.40 A 32-483 [» ]
    3FCS X-ray 2.55 A/C 32-989 [» ]
    3FCU X-ray 2.90 A/C/E 32-488 [» ]
    3NID X-ray 2.30 A/C 32-488 [» ]
    3NIF X-ray 2.40 A/C 32-488 [» ]
    3NIG X-ray 2.25 A/C 32-488 [» ]
    3T3M X-ray 2.60 A/C 32-488 [» ]
    3T3P X-ray 2.20 A/C 32-488 [» ]
    3ZDX X-ray 2.45 A/C 32-488 [» ]
    3ZDY X-ray 2.45 A/C 32-488 [» ]
    3ZDZ X-ray 2.75 A/C 32-488 [» ]
    3ZE0 X-ray 2.95 A/C 32-488 [» ]
    3ZE1 X-ray 3.00 A/C 32-488 [» ]
    3ZE2 X-ray 2.35 A/C 32-488 [» ]
    4CAK electron microscopy 20.50 A 32-989 [» ]
    ProteinModelPortali P08514.
    SMRi P08514. Positions 32-989, 991-1039.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109881. 10 interactions.
    DIPi DIP-68N.
    IntActi P08514. 1 interaction.
    STRINGi 9606.ENSP00000262407.

    Chemistry

    BindingDBi P08514.
    ChEMBLi CHEMBL2111443.
    DrugBanki DB00775. Tirofiban.

    PTM databases

    PhosphoSitei P08514.

    Polymorphism databases

    DMDMi 226694183.

    2D gel databases

    OGPi P08514.

    Proteomic databases

    PaxDbi P08514.
    PRIDEi P08514.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000262407 ; ENSP00000262407 ; ENSG00000005961 . [P08514-1 ]
    GeneIDi 3674.
    KEGGi hsa:3674.
    UCSCi uc002igt.1. human. [P08514-1 ]

    Organism-specific databases

    CTDi 3674.
    GeneCardsi GC17M042460.
    HGNCi HGNC:6138. ITGA2B.
    HPAi CAB018611.
    HPA031168.
    HPA031169.
    HPA031170.
    HPA031171.
    MIMi 187800. phenotype.
    273800. phenotype.
    607759. gene.
    neXtProti NX_P08514.
    Orphaneti 140957. Autosomal dominant macrothrombocytopenia.
    853. Fetal and neonatal alloimmune thrombocytopenia.
    849. Glanzmann thrombasthenia.
    PharmGKBi PA29938.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG26407.
    HOGENOMi HOG000231603.
    HOVERGENi HBG006186.
    InParanoidi P08514.
    KOi K06476.
    OMAi CFNIQMC.
    OrthoDBi EOG7TMZQZ.
    PhylomeDBi P08514.
    TreeFami TF105391.

    Enzyme and pathway databases

    Reactomei REACT_13552. Integrin cell surface interactions.
    REACT_15381. p130Cas linkage to MAPK signaling for integrins.
    REACT_15523. Integrin alphaIIb beta3 signaling.
    REACT_163906. ECM proteoglycans.
    REACT_22272. Signal transduction by L1.
    SignaLinki P08514.

    Miscellaneous databases

    EvolutionaryTracei P08514.
    GeneWikii ITGA2B.
    GenomeRNAii 3674.
    NextBioi 14381.
    PMAP-CutDB Q17R67.
    PROi P08514.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P08514.
    Bgeei P08514.
    CleanExi HS_ITGA2B.
    Genevestigatori P08514.

    Family and domain databases

    InterProi IPR013517. FG-GAP.
    IPR013519. Int_alpha_beta-p.
    IPR000413. Integrin_alpha.
    IPR013649. Integrin_alpha-2.
    IPR018184. Integrin_alpha_C_CS.
    [Graphical view ]
    Pfami PF01839. FG-GAP. 1 hit.
    PF00357. Integrin_alpha. 1 hit.
    PF08441. Integrin_alpha2. 1 hit.
    [Graphical view ]
    PRINTSi PR01185. INTEGRINA.
    SMARTi SM00191. Int_alpha. 5 hits.
    [Graphical view ]
    PROSITEi PS51470. FG_GAP. 7 hits.
    PS00242. INTEGRIN_ALPHA. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Structure of the platelet membrane glycoprotein IIb. Homology to the alpha subunits of the vitronectin and fibronectin membrane receptors."
      Poncz M., Eisman R., Heidenreich R., Silver S.M., Vilaire G., Surrey S., Schwartz E., Bennett J.S.
      J. Biol. Chem. 262:8476-8482(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ALA-313.
    2. "GPIIb and GPIIIa amino acid sequences deduced from human megakaryocyte cDNAs."
      Frachet P., Uzan G., Thevenon D., Denarier E., Prandini M.H., Marguerie G.
      Mol. Biol. Rep. 14:27-33(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ALA-313.
    3. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
    4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Spleen.
    5. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
      Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L.
      , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
      Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Lung.
    7. "Human platelets and megakaryocytes contain alternately spliced glycoprotein IIb mRNAs."
      Bray P.F., Leung C.S.-I., Shuman M.A.
      J. Biol. Chem. 265:9587-9590(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2).
      Tissue: Erythroleukemia.
    8. "cDNA clones for human platelet GPIIb corresponding to mRNA from megakaryocytes and HEL cells. Evidence for an extensive homology to other Arg-Gly-Asp adhesion receptors."
      Uzan G., Frachet P., Lajmanovich A., Prandini M.-H., Denarier E., Duperray A., Loftus J., Ginsberg M., Plow E., Marguerie G.
      Eur. J. Biochem. 171:87-93(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 392-1039 (ISOFORM 1).
    9. "Platelet glycoprotein IIb. Chromosomal localization and tissue expression."
      Bray P.F., Rosa J.P., Johnston G.I., Shiu D.T., Cook R.G., Lau C., Kan Y.W., McEver R.P., Shuman M.A.
      J. Clin. Invest. 80:1812-1817(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 868-1039 (ISOFORM 1).
    10. "Isolation of the human platelet glycoprotein IIb gene and characterization of the 5' flanking region."
      Prandini M.H., Denarier E., Frachet P., Uzan G., Marguerie G.
      Biochem. Biophys. Res. Commun. 156:595-601(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-62 AND 1021-1039.
    11. "Platelet glycoproteins IIb and IIIa: evidence for a family of immunologically and structurally related glycoproteins in mammalian cells."
      Charo I.F., Fitzgerald L.A., Steiner B., Rall S.C., Bekeart L.S., Phillips D.R.
      Proc. Natl. Acad. Sci. U.S.A. 83:8351-8355(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 32-56 AND 903-917.
    12. "Separation of important new platelet glycoproteins (GPIa, GPIc, GPIc*, GPIIa and GMP-140) by F.P.L.C. Characterization by monoclonal antibodies and gas-phase sequencing."
      Catimel B., Parmentier S., Leung L.L., McGregor J.L.
      Biochem. J. 279:419-425(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 32-42.
    13. "Thermal stability of individual domains in platelet glycoprotein IIbIIIa."
      Makogonenko E.M., Yakubenko V.P., Ingham K.C., Medved L.V.
      Eur. J. Biochem. 237:205-211(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 32 AND 872.
    14. "Purification and partial amino acid sequence of human platelet membrane glycoproteins IIb and IIIa."
      Hiraiwa A., Matsukage A., Shiku H., Takahashi T., Naito K., Yamada K.
      Blood 69:560-564(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 487-501 AND 1026-1038.
    15. "Interchain and intrachain disulphide bonds in human platelet glycoprotein IIb. Localization of the epitopes for several monoclonal antibodies."
      Calvete J.J., Alvarez M.V., Rivas G., Hew C.L., Henschen A., Gonzalez-Rodriguez J.
      Biochem. J. 261:551-560(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 903-922 AND 934-939.
    16. "Complete localization of the intrachain disulphide bonds and the N-glycosylation points in the alpha-subunit of human platelet glycoprotein IIb."
      Calvete J.J., Henschen A., Gonzalez-Rodriguez J.
      Biochem. J. 261:561-568(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL PROTEIN SEQUENCE, DISULFIDE BONDS, GLYCOSYLATION AT ASN-46; ASN-280; ASN-601 AND ASN-711.
    17. "Localization of an O-glycosylation site in the alpha-subunit of the human platelet integrin GPIIb/IIIa involved in Baka (HPA-3a) alloantigen expression."
      Calvete J.J., Muniz-Diaz E.
      FEBS Lett. 328:30-34(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL PROTEIN SEQUENCE, GLYCOSYLATION AT SER-878.
    18. "Identification of a novel truncated alphaIIb integrin."
      Trikha M., Cai Y., Grignon D., Honn K.V.
      Cancer Res. 58:4771-4775(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
    19. "Characterization of the beta-chain N-terminus heterogeneity and the alpha-chain C-terminus of human platelet GPIIb. Posttranslational cleavage sites."
      Calvete J.J., Schafer W., Henschen A., Gonzalez-Rodriguez J.
      FEBS Lett. 272:37-40(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEOLYTIC CLEAVAGE, PYROGLUTAMATE FORMATION AT GLN-891.
    20. "Identification of a novel calcium-binding protein that interacts with the integrin alphaIIb cytoplasmic domain."
      Naik U.P., Patel P.M., Parise L.V.
      J. Biol. Chem. 272:4651-4654(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CIB1.
      Tissue: Fetal liver.
    21. "Calcium-dependent properties of CIB binding to the integrin alphaIIb cytoplasmic domain and translocation to the platelet cytoskeleton."
      Shock D.D., Naik U.P., Brittain J.E., Alahari S.K., Sondek J., Parise L.V.
      Biochem. J. 342:729-735(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CIB1.
    22. "Bidirectional transmembrane modulation of integrin alphaIIbbeta3 conformations."
      Leisner T.M., Wencel-Drake J.D., Wang W., Lam S.C.
      J. Biol. Chem. 274:12945-12949(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF 1029-PRO-PRO-1030.
    23. "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
      Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
      J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-601.
      Tissue: Plasma.
    24. "RN181, a novel ubiquitin E3 ligase that interacts with the KVGFFKR motif of platelet integrin alpha(IIb)beta3."
      Brophy T.M., Raab M., Daxecker H., Culligan K.G., Lehmann I., Chubb A.J., Treumann A., Moran N.
      Biochem. Biophys. Res. Commun. 369:1088-1093(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RNF181.
    25. "Solution structures of Ca2+-CIB1 and Mg2+-CIB1 and their interactions with the platelet integrin alphaIIb cytoplasmic domain."
      Huang H., Ishida H., Yamniuk A.P., Vogel H.J.
      J. Biol. Chem. 286:17181-17192(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CIB1.
    26. "Biophysical and structural studies of the human calcium- and integrin-binding protein family: understanding their functional similarities and differences."
      Huang H., Bogstie J.N., Vogel H.J.
      Biochem. Cell Biol. 90:646-656(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CIB1; CIB2; CIB3 AND CIB4.
    27. "Structural basis for the activation of platelet integrin alphaIIbbeta3 by calcium- and integrin-binding protein 1."
      Huang H., Vogel H.J.
      J. Am. Chem. Soc. 134:3864-3872(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CIB1.
    28. "Inherited diseases of platelet glycoproteins: considerations for rapid molecular characterization."
      Bray P.F.
      Thromb. Haemost. 72:492-502(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON GT VARIANTS.
    29. "Polymorphism of human platelet membrane glycoprotein IIb associated with the Baka/Bakb alloantigen system."
      Lyman S., Aster R.H., Visentin G.P., Newman P.J.
      Blood 75:2343-2348(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT HPA-3 (BAK).
    30. "Glanzmann thrombasthenia secondary to a Gly273-->Asp mutation adjacent to the first calcium-binding domain of platelet glycoprotein IIb."
      Poncz M., Rifat S., Coller B.S., Newman P.J., Shattil S.J., Parrella T., Fortina P., Bennett J.S.
      J. Clin. Invest. 93:172-179(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT GT ASP-273.
    31. "A single amino acid substitution flanking the fourth calcium binding domain of alpha IIb prevents maturation of the alpha IIb beta 3 integrin complex."
      Wilcox D.A., Wautier J.-L., Pidard D., Newman P.J.
      J. Biol. Chem. 269:4450-4457(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT GT ASP-449.
    32. "Glanzmann thrombasthenia resulting from a single amino acid substitution between the second and third calcium-binding domains of GPIIb. Role of the GPIIb amino terminus in integrin subunit association."
      Wilcox D.A., Paddock C.M., Lyman S., Gill J.C., Newman P.J.
      J. Clin. Invest. 95:1553-1560(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT GT HIS-358.
    33. "Glanzmann thrombasthenia due to a two amino acid deletion in the fourth calcium-binding domain of alpha IIb: demonstration of the importance of calcium-binding domains in the conformation of alpha IIb beta 3."
      Basani R.B., Vilaire G., Shattil S.J., Kolodziej M.A., Bennett J.S., Poncz M.
      Blood 88:167-173(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT GT VAL-456-457-ASP DEL, CHARACTERIZATION OF VARIANT GT VAL-456-457-ASP DEL.
    34. "Hematologically important mutations: Glanzmann thrombasthenia."
      French D.L., Coller B.S.
      Blood Cells Mol. Dis. 23:39-51(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS GT ILE-207; THR-596 AND GLN-1026.
    35. "Glycoprotein IIb Leu214Pro mutation produces Glanzmann thrombasthenia with both quantitative and qualitative abnormalities in GPIIb/IIIa."
      Grimaldi C.M., Chen F., Wu C., Weiss H.J., Coller B.S., French D.L.
      Blood 91:1562-1571(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT GT PRO-214, CHARACTERIZATION OF VARIANT GT PRO-214.
    36. "A Gln747-->Pro substitution in the IIb subunit is responsible for a moderate IIbbeta3 deficiency in Glanzmann thrombasthenia."
      Tadokoro S., Tomiyama Y., Honda S., Arai M., Yamamoto N., Shiraga M., Kosugi S., Kanakura Y., Kurata Y., Matsuzawa Y.
      Blood 92:2750-2758(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT GT PRO-778.
    37. "R to Q amino acid substitution in the GFFKR sequence of the cytoplasmic domain of the integrin IIb subunit in a patient with a Glanzmann's thrombasthenia-like syndrome."
      Peyruchaud O., Nurden A.T., Milet S., Macchi L., Pannochia A., Bray P.F., Kieffer N., Bourre F.
      Blood 92:4178-4187(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT BDPLT16 GLN-1026, CHARACTERIZATION OF VARIANT BDPLT16 GLN-1026.
    38. "Novel point mutations in the alphaIIb subunit (Phe289-->Ser, Glu324-->Lys and Gln747-->Pro) causing thrombasthenic phenotypes in four Japanese patients."
      Ambo H., Kamata T., Handa M., Kawai Y., Oda A., Murata M., Takada Y., Ikeda Y.
      Br. J. Haematol. 102:829-840(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS GT SER-320; LYS-355 AND PRO-778.
    39. "Double heterozygosity of the GPIIb gene in a Swiss patient with Glanzmann's thrombasthenia."
      Ruan J., Peyruchaud O., Alberio L., Valles G., Clemetson K., Bourre F., Nurden A.T.
      Br. J. Haematol. 102:918-925(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS GT LYS-355 AND THR-596.
    40. Cited for: VARIANTS ILE-40; SER-874 AND ASN-968.
    41. "Molecular genetic analysis of a compound heterozygote for the glycoprotein (GP) IIb gene associated with Glanzmann's thrombasthenia: disruption of the 674-687 disulfide bridge in GPIIb prevents surface exposure of GPIIb-IIIa complexes."
      Gonzalez-Manchon C., Fernandez-Pinel M., Arias-Salgado E.G., Ferrer M., Alvarez M.-V., Garcia-Munoz S., Ayuso M.S., Parrilla R.
      Blood 93:866-875(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT GT ARG-705, CHARACTERIZATION OF VARIANT GT ARG-705.
    42. "A naturally occurring mutation near the amino terminus of alphaIIb defines a new region involved in ligand binding to alphaIIbbeta3."
      Basani R.B., French D.L., Vilaire G., Brown D.L., Chen F., Coller B.S., Derrick J.M., Gartner T.K., Bennett J.S., Poncz M.
      Blood 95:180-188(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS GT ALA-176 AND LEU-176.
    43. "Description of 10 new mutations in platelet glycoprotein IIb (alphaIIb) and glycoprotein IIIa (beta3) genes."
      Vinciguerra C., Bordet J.C., Beaune G., Grenier C., Dechavanne M., Negrier C.
      Platelets 12:486-495(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS GT TRP-161; LEU-222; ARG-412 AND PRO-847.
    44. "A Leu55 to Pro substitution in the integrin alphaIIb is responsible for a case of Glanzmann's thrombasthenia."
      Tanaka S., Hayashi T., Hori Y., Terada C., Han K.S., Ahn H.S., Bourre F., Tani Y.
      Br. J. Haematol. 118:833-835(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT GT PRO-86, CHARACTERIZATION OF VARIANT GT PRO-86.
    45. "Glanzmann's thrombasthenia: identification of 19 new mutations in 30 patients."
      D'Andrea G., Colaizzo D., Vecchione G., Grandone E., Di Minno G., Margaglione M.
      Thromb. Haemost. 87:1034-1042(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS GT VAL-139; ALA-176; GLU-267; ASP-380; THR-405; ASP-581; ARG-705; VAL-752 AND PRO-755.
    46. "Two novel mutations in the alpha IIb calcium-binding domains identify hydrophobic regions essential for alpha IIbbeta 3 biogenesis."
      Mitchell W.B., Li J.H., Singh F., Michelson A.D., Bussel J., Coller B.S., French D.L.
      Blood 101:2268-2276(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS GT PHE-329 AND THR-405, CHARACTERIZATION OF VARIANTS GT PHE-329 AND THR-405.
    47. "A naturally occurring Tyr143His alpha IIb mutation abolishes alpha IIb beta 3 function for soluble ligands but retains its ability for mediating cell adhesion and clot retraction: comparison with other mutations causing ligand-binding defects."
      Kiyoi T., Tomiyama Y., Honda S., Tadokoro S., Arai M., Kashiwagi H., Kosugi S., Kato H., Kurata Y., Matsuzawa Y.
      Blood 101:3485-3491(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT GT HIS-174, CHARACTERIZATION OF VARIANT GT HIS-174.
    48. "Triple heterozygosity in the integrin alphaIIb subunit in a patient with Glanzmann's thrombasthenia."
      Nurden A.T., Breillat C., Jacquelin B., Combrie R., Freedman J., Blanchette V.S., Schmugge M., Rand M.L.
      J. Thromb. Haemost. 2:813-819(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT GT MET-982, CHARACTERIZATION OF VARIANT GT MET-982, VARIANT THR-989.
    49. "A novel Phe171Cys mutation in integrin alpha causes Glanzmann thrombasthenia by abrogating alphaIIbbeta3 complex formation."
      Rosenberg N., Landau M., Luboshitz J., Rechavi G., Seligsohn U.
      J. Thromb. Haemost. 2:1167-1175(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT GT CYS-202, CHARACTERIZATION OF VARIANT GT CYS-202.
    50. "Type II Glanzmann thrombasthenia in a compound heterozygote for the alpha IIb gene. A novel missense mutation in exon 27."
      Jayo A., Pabon D., Lastres P., Jimenez-Yuste V., Gonzalez-Manchon C.
      Haematologica 91:1352-1359(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT GT LEU-943, CHARACTERIZATION OF VARIANT GT LEU-943.
    51. "AlphaIIbbeta3 integrin: new allelic variants in Glanzmann thrombasthenia, effects on ITGA2B and ITGB3 mRNA splicing, expression, and structure-function."
      Jallu V., Dusseaux M., Panzer S., Torchet M.F., Hezard N., Goudemand J., de Brevern A.G., Kaplan C.
      Hum. Mutat. 31:237-246(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS GT THR-405; THR-596; ARG-705; PRO-778; PHE-934; LEU-957; MET-982 AND THR-989, CHARACTERIZATION OF VARIANTS GT PHE-934 AND LEU-957.
    52. "Heterozygous ITGA2B R995W mutation inducing constitutive activation of the alphaIIbbeta3 receptor affects proplatelet formation and causes congenital macrothrombocytopenia."
      Kunishima S., Kashiwagi H., Otsu M., Takayama N., Eto K., Onodera M., Miyajima Y., Takamatsu Y., Suzumiya J., Matsubara K., Tomiyama Y., Saito H.
      Blood 117:5479-5484(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT BDPLT16 TRP-1026, CHARACTERIZATION OF VARIANT BDPLT16 TRP-1026.

    Entry informationi

    Entry nameiITA2B_HUMAN
    AccessioniPrimary (citable) accession number: P08514
    Secondary accession number(s): B2RCY8
    , O95366, Q14443, Q17R67
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1988
    Last sequence update: April 14, 2009
    Last modified: October 1, 2014
    This is version 190 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human cell differentiation molecules
      CD nomenclature of surface proteins of human leucocytes and list of entries
    2. Human chromosome 17
      Human chromosome 17: entries, gene names and cross-references to MIM
    3. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    4. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    5. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    6. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3